Journal
SCIENTIFIC REPORTS
Volume 3, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/srep03178
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Funding
- JSPS Research Fellowship for Young Scientists
- Young Scientists, and Scientific Research on Innovative Areas [3308]
- Ministry of Education, Culture, Science, Sports, and Technology (MEXT)
- global health issues from theMinistry of Health, Labour andWelfare of Japan
- Bio-oriented Technology Research Advancement Institution (BRAIN)
- Grants-in-Aid for Scientific Research [24688032, 24117506] Funding Source: KAKEN
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Heparin, a sulfated glycoconjugate, reportedly inhibits the blood-stage growth of the malaria parasite Plasmodium falciparum. Elucidation of the inhibitory mechanism is valuable for developing novel invasion-blocking treatments based on heparin. Merozoite surface protein 1 has been reported as a candidate target of heparin; however, to better understand the molecular mechanisms involved, we characterized the molecules that bind to heparin during merozoite invasion. Here, we show that heparin binds only at the apical tip of the merozoite surface and that multiple heparin-binding proteins localize preferentially in the apical organelles. To identify heparin-binding proteins, parasite proteins were fractionated by means of heparin affinity chromatography and subjected to immunoblot analysis with ligand-specific antibodies. All tested members of the Duffy and reticulocyte binding-like families bound to heparin with diverse affinities. These findings suggest that heparin masks the apical surface of merozoites and blocks interaction with the erythrocyte membrane after initial attachment.
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